@article{534cd67f33ba4428939b9b71bc22f594,
title = "Type I chaperonins: Not all are created equal",
abstract = "Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. Since their discovery, the bacterial chaperonins have provided an excellent model system for investigating the mechanism by which chaperonins mediate protein folding. Due to the high conservation of the primary sequence among Type I chaperonins, it is generally accepted that organellar chaperonins function similar to the bacterial ones. However, recent studies indicate that the chloroplast and mitochondrial chaperonins possess unique structural and functional properties that distinguish them from their bacterial homologs. This review focuses on the unique properties of organellar chaperonins.",
keywords = "Chaperonin, GroEL, GroES, Type I chaperonin, cpn10, cpn60",
author = "Galit Levy-Rimler and Bell, {Rachel E.} and Nir Ben-Tal and Abdussalam Azem",
note = "Funding Information: We thank Dr. Celeste Weiss for critical review of this manuscript. A.A. was supported by grants from G.I.F. (German-Israeli Foundation for Research and Development) young scientists program and from the United States–Israel Binational Science Foundation.",
year = "2002",
month = oct,
day = "2",
doi = "10.1016/S0014-5793(02)03178-2",
language = "אנגלית",
volume = "529",
pages = "1--5",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "1",
}